A collagen hydrolysate/milk protein-blend stimulates muscle anabolism equivalently to an isoenergetic milk protein-blend containing a greater quantity of essential amino acids in older men

Abstract

Background & aims: Nutritional composition is key for skeletal muscle maintenance into older age. Yet the acute effects of collagen protein blended with other protein sources, in relation to skeletal muscle anabolism, are ill-defined. We investigated human muscle protein synthesis (MPS) responses to a 20 g blend of collagen protein hydrolysate þ milk protein (CPþMP, 125 ml) oral nutritional supplement (ONS) vs. 20 g non-blended milk protein source (MP, 200 ml) ONS, in older adults. Methods: Healthy older men (N ¼ 8, 71±1 y, BMI: 27±1 kg$m À2 ) underwent a randomized trial of 20 g protein, from either a CPþMP blend (Fresubin®3.2 kcal DRINK), or a kcal-matched (higher in essential amino acids (EAA) ONS of MP alone. Vastus lateralis (VL) MPS and plasma AA were determined using stable isotope-tracer mass spectrometry; anabolic signaling was quantified via immuno-blotting in VL biopsies taken at baseline and 2/4 h after ONS feeding. Plasma insulin was measured via enzyme-linked immunosorbent assay (ELISA). Measures were taken at rest, after the feed (FED) and after the feed þ exercise (FED-EX) conditions (unilateral leg exercise, 6 Â 8, 75% 1-RM).Results: MP resulted in a greater increase in plasma leucine (MP mean: 152 ± 6 mM, CPþMP mean: 113 ± 4 mM (Feed P < 0.001) and EAA (MP mean: 917 ± 25 mM, CPþMP mean: 786 ± 15 mM (Feed P < 0.01) than CPþMP. CP þ MP increased plasma glycine (peak 385 ± 57 mM (P < 0.05)), proline (peak 323 ± 29 mM (P < 0.01)) and non-essential amino acids (NEAA) (peak 1621 ± 107 mM (P < 0.01)) with MP showing no increase. Plasma insulin increased in both trials (CPþMP: 58 ± 10 mU/mL (P < 0.01), MP: 42 ± 6 mU/mL (P < 0.01), with peak insulin greater with CPþMP vs. MP (P < 0.01). MPS demonstrated equivalent increases in response to CPþMP and MP under both FED (MP: 0.

Association of postprandial postexercise muscle protein synthesis rates with dietary leucine: A systematic review

“…Figure 1 shows the process of article selection with 38 studies ultimately included. Within these 38 studies, there were 77 study arms (i.e., total number of eligible intervention groups), to determine aspects relating to the leucine threshold hypothesis (Supplementary Information—https://doi.org/10.6084/m9.figshare.22203514, Agergaard et al, 2017; Areta et al, 2014; Atherton et al, 2017; Beals et al, 2018; Borack et al, 2016; Brook et al, 2021; Bukhari et al, 2015; Burd et al, 2010, 2015; Burd, Andrews, et al, 2012; Burd, Yang, et al, 2012; Chan et al, 2019; Churchward‐Venne, Breen, et al, 2014; Churchward‐Venne, Cotie, et al, 2014; Devries et al, 2018a, 2018b; Dickinson et al, 2014; Dideriksen et al, 2016; Dreyer et al, 2008; Fujita et al, 2009; Gwin et al, 2021; Hermans et al, 2021, 2022; Luiking et al, 2014; McGlory et al, 2016; McKendry et al, 2016; Mikkelsen et al, 2015; Monteyne, Coelho, Porter, Abdelrahman, Jameson, Finnigan, et al, 2020; Monteyne, Coelho, Porter, Abdelrahman, Jameson, Jackman, et al, 2020; Moore, Tang, et al, 2009; Oikawa et al, 2020; Pinckaers et al, 2022; Reidy et al, 2013; Reitelseder et al, 2019; Symons et al, 2011; Van Vliet et al, 2017; West et al, 2009; Wilkinson et al, 2018). Studies which met all the inclusion criteria except not taking a basal muscle biopsy (i.e., Dideriksen et al, 2011) were excluded in order to calculate delta change from basal MPS.…”

“…Protein ingestion before (Burke et al, 2012; Tipton et al, 2007), immediately after (Brook et al, 2021; Moore, Robinson, et al, 2009; Pennings, Koopman, et al, 2011; Tang et al, 2009), and up to 24‐h (Elliot et al, 2006; Holwerda et al, 2016; Kim et al, 2016) postresistance exercise augments the rise in MPS rates and, albeit less potently, inhibits MPB rates (Biolo et al, 1997) resulting in a positive net muscle protein balance. The magnitude of the (postexercise) MPS response to protein ingestion appears to increase in a dose–response manner plateauing somewhere between 20 and 40 g (Moore, Robinson, et al, 2009; Witard et al, 2014; Yang et al, 2012), a relationship that shifts to the right in more anabolically insensitive older adults (Burd et al, 2013; Cuthbertson et al, 2005; Rennie & Wilkes, 2005; Wall, Gorissen, et al, 2015).…”

Advances in muscle health and nutrition: A toolkit for healthcare professionals

“…Collagen is rich in nonessential amino acids, which may explain its positive effects on nitrogen balance [165]. Moreover, a mixed blend of collagen and milk protein induced MPS to a similar extent as milk protein alone, and also exhibited a greater increases in mammalian target of rapamycin (mTOR) signaling in spite of lower leucine content [175].…”

Protein Requirements for Master Athletes: Just Older Versions of Their Younger Selves

“…While other supplements have been investigated for their potential role in preventing or facilitating recovery from injuries, the reader is referred to other reviews on this topic [ 158 ]. Thus, while collagen protein, due to its primary nonessential amino acid profile and low protein score [ 159 ], does not support contractile protein remodeling in humans [ 160 , 161 ], it may be paired with other higher quality proteins to augment MyoPS [ 162 ]. However, preliminary research suggests that collagen supplementation may not enhance muscle extracellular matrix remodeling with exercise in older women [ 161 ], although the large variability in muscle collagen protein synthesis and moderate estimated effect size (i.e.…”